Reviewed, UniProtKB/Swiss-Prot P20618 (PSB1_HUMAN)

Names and origin

Protein names

Recommended name:
    Proteasome subunit beta type-1
    EC=3.4.25.1
Alternative name(s):
    Proteasome component C5
    Macropain subunit C5
    Multicatalytic endopeptidase complex subunit C5
    Proteasome gamma chain

Gene names

Name:	PSMB1
Synonyms:	PSC5

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the peptidase T1B family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP4	P49662	1	EBI-372273,EBI-1057327
DCP2	Q8IU60	1	EBI-372273,EBI-521577
DSTYK	Q6XUX3	1	EBI-372273,EBI-1049520
PASK	Q96RG2	1	EBI-372273,EBI-1042651
RIOK3	O14730	1	EBI-372273,EBI-1047061
VHL	P40337	1	EBI-372273,EBI-301246

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 28	28	Ref.6		PRO_0000259623
	Chain	29 – 241	213	Proteasome subunit beta type-1		PRO_0000148030
Amino acid modifications
	Modified residue	150	1	Phosphotyrosine By similarity
Natural variations
	Natural variant	11	1	P → A: dbSNP rs12717. Ref.5		VAR_051547
	Natural variant	208	1	I → N: dbSNP rs10541.		VAR_051548

Sequences

	Sequence		Length	Mass (Da)
	P20618-1 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: AE8FC42799F39157	FASTA	241	26,489
	10 20 30 40 50 60 MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI VASDTRLSEG 70 80 90 100 110 120 FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL KMYKHSNNKA MTTGAIAAML 130 140 150 160 170 180 STILYSRRFF PYYVYNIIGG LDEEGKGAVY SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ 190 200 210 220 230 240 VGFKNMQNVE HVPLSLDRAM RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)." Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A. Biochim. Biophys. Acta 1089:95-102(1991) [PubMed: 2025653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-11. Tissue: Brain and Lung.
[6]	"Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)." Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A. Biochim. Biophys. Acta 1037:178-185(1990) [PubMed: 2306472] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-52.
[7]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed: 17323924] [Abstract] Cited for: PROTEOLYTIC PROCESSING [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00761 mRNA. Translation: BAA00658.1. BT019720 mRNA. Translation: AAV38525.1. AB451312 mRNA. Translation: BAG70126.1. AB451442 mRNA. Translation: BAG70256.1. AL031259 Genomic DNA. Translation: CAA20287.1. BC000508 mRNA. Translation: AAH00508.1. BC020807 mRNA. Translation: AAH20807.1.
IPI	IPI00025019.
PIR	SNHUC5. S15973.
RefSeq	NP_002784.1.
UniGene	Hs.352768 Hs.590872
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P23724.
SMR	P20618. Positions 29-241.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20618. 24 interactions.
Protein family/group databases
MEROPS	T01.986.
PTM databases
PhosphoSite	P20618.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00025019.
Proteomic databases
PeptideAtlas	P20618.
PRIDE	P20618.
Genome annotation databases
Ensembl	ENSG00000008018. Homo sapiens. [Contig view]
GeneID	5689.
KEGG	hsa:5689.
UCSC	uc003qxr.1. human.
Organism-specific databases
GeneCards	GC06M170761.
H-InvDB	HIX0006400.
HGNC	HGNC:9537. PSMB1.
MIM	602017. gene.
PharmGKB	PA33882.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P20618.
HOVERGEN	P20618.
OMA	P20618. EREQCRA.
Enzyme and pathway databases
BRENDA	3.4.25.1. 247.
Reactome	REACT_11045. Signaling by Wnt. REACT_13. Metabolism of amino acids. REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	P20618.
Bgee	P20618.
CleanEx	HS_PSMB1.
GermOnline	ENSG00000008018. Homo sapiens.
Family and domain databases
InterPro	IPR001353. Proteasome_alpha_beta_su. IPR016050. Proteasome_bsu_CS. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PROSITE	PS00854. PROTEASOME_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00188. Bortezomib.
NextBio	22098.
SOURCE	Search...

Entry information

Entry name

PSB1_HUMAN

Accession

Primary (citable) accession number: P20618
Secondary accession number(s): B5BU76, Q9BWA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 1, 1992
Last modified:	July 7, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)